Palmitate-induced PTP1B expression is mediated by ceramide-JNK and nuclear factor κB (NF-κB) activation

Mohammadtaghvaei, Narges; Taheripak, Gholamreza; Taghikhani, Mohammad; Meshkani, Reza

doi:10.1016/j.cellsig.2012.04.019

Cited by 38 publications

(28 citation statements)

References 37 publications

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“…Interestingly, a putative cis-regulatory element for NFκB binding site has been previously identified within the Ptp1b promoter [45]. Additionally the p65 subunit of NFκB has been shown to bind and activate Ptp1b promoter in response to TNFα treatment in a liver of mice [11].…”

Section: Resultsmentioning

confidence: 99%

“…Since ROS are capable of activating NFκB signaling pathway, mainly through the classical IKK-dependent pathway [44], [54], we hypothesized that the ER stress-induced ROS leads to the induction of NFκB pathway. It also has been shown that Ptp1 b promoter has NFκB binding site and that PTP1B expression is induced by inflammation through activation of NFκB pathway [11], [45]. So we further investigated NFκB as a possible candidate responsible for ER stress-induced PTP1B expression.…”

Section: Discussionmentioning

confidence: 95%

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Protein Tyrosine Phosphatase 1B and Insulin Resistance: Role of Endoplasmic Reticulum Stress/Reactive Oxygen Species/Nuclear Factor Kappa B Axis

2013

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Obesity-induced endoplasmic reticulum (ER) stress has been proposed as an important pathway in the development of insulin resistance. Protein-tyrosine phosphatase 1B (PTP1B) is a negative regulator of insulin signaling and is tethered to the ER-membrane. The aim of the study was to determine the mechanisms involved in the crosstalk between ER-stress and PTP1B. PTP1B whole body knockout and C57BL/6J mice were subjected to a high-fat or normal chow-diet for 20 weeks. High-fat diet feeding induced body weight gain, increased adiposity, systemic glucose intolerance, and hepatic steatosis were attenuated by PTP1B deletion. High-fat diet- fed PTP1B knockout mice also exhibited improved glucose uptake measured using [3H]-2-deoxy-glucose incorporation assay and Akt phosphorylation in the skeletal muscle tissue, compared to their wild-type control mice which received similar diet. High-fat diet-induced upregulation of glucose-regulated protein-78, phosphorylation of eukaryotic initiation factor 2α and c-Jun NH2-terminal kinase-2 were significantly attenuated in the PTP1B knockout mice. Mice lacking PTP1B showed decreased expression of the autophagy related protein p62 and the unfolded protein response adaptor protein NCK1 (non-catalytic region of tyrosine kinase). Treatment of C2C12 myotubes with the ER-stressor tunicamycin resulted in the accumulation of reactive oxygen species (ROS), leading to the activation of protein expression of PTP1B. Furthermore, tunicamycin-induced ROS production activated nuclear translocation of NFκB p65 and was required for ER stress-mediated expression of PTP1B. Our data suggest that PTP1B is induced by ER stress via the activation of the ROS-NFκB axis which is causes unfolded protein response and mediates insulin resistance in the skeletal muscle under obese condition.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 95%

Protein Tyrosine Phosphatase 1B and Insulin Resistance: Role of Endoplasmic Reticulum Stress/Reactive Oxygen Species/Nuclear Factor Kappa B Axis

2013

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“…Mahadev et al (246) reported that NADPH oxidase-induced H 2 O 2 enhances insulin signaling via oxidative inhibition of PTPs. Furthermore, palmitate-induced insulin resistance in rat skeletal muscle occurs through increased activity of PTPs via JNK and NF-κB (250), which is reversed 16 h after acute exercise in rats (222). Loh et al (54) revealed that the elevated H 2 O 2 response to insulin in GPx1 −/− mouse embryo fibroblasts coincided with elevated PI3K/Akt signaling, which can be suppressed by pretreating cells with ebselen, an NADPH oxidase inhibitor, or the antioxidant N -acetylcysteine.…”

Section: Positive and Negative Regulation Of Glycemic Control By Rosmentioning

confidence: 99%

Exercise and Glycemic Control: Focus on Redox Homeostasis and Redox-Sensitive Protein Signaling

et al. 2017

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Physical inactivity, excess energy consumption, and obesity are associated with elevated systemic oxidative stress and the sustained activation of redox-sensitive stress-activated protein kinase (SAPK) and mitogen-activated protein kinase signaling pathways. Sustained SAPK activation leads to aberrant insulin signaling, impaired glycemic control, and the development and progression of cardiometabolic disease. Paradoxically, acute exercise transiently increases oxidative stress and SAPK signaling, yet postexercise glycemic control and skeletal muscle function are enhanced. Furthermore, regular exercise leads to the upregulation of antioxidant defense, which likely assists in the mitigation of chronic oxidative stress-associated disease. In this review, we explore the complex spatiotemporal interplay between exercise, oxidative stress, and glycemic control, and highlight exercise-induced reactive oxygen species and redox-sensitive protein signaling as important regulators of glucose homeostasis.

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“…However, the target molecules for FFAs in insulin signaling are not completely understood. We have recently demonstrated that palmitate can induce insulin resistance in muscle cells by enhancing the expression of PTP1B (MohammadTaghvaei et al 2011(MohammadTaghvaei et al , 2012. In this study, we provided more evidence that LAR is also a new mediator of palmitate-induced muscle insulin resistance.…”

Section: Discussionmentioning

confidence: 57%

Leukocyte antigen-related inhibition attenuates palmitate-induced insulin resistance in muscle cells

Gorgani‐Firuzjaee¹,

Bakhtiyari²,

Golestani³

et al. 2012

Journal of Endocrinology

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Palmitate has been shown to induce insulin resistance in skeletal muscle cells. The aim of this study was to investigate the role of the leukocyte common antigen-related (LAR) gene in palmitate-induced insulin resistance in C2C12 cells. A stable C2C12 cell line was generated using LAR short hairpin RNA. The levels of LAR protein and phosphorylation of insulin receptor substrate-1 (IRS1) and Akt were detected by western blot analysis. 2-Deoxyglucose uptake was measured in LAR knockdown and control cells using D-[2- significantly induced LAR mRNA (65%) and protein levels (40%) in myotubes compared with untreated cells. Palmitate significantly reduced insulin-stimulated glucose uptake in both the control and LAR knockdown cells by 33 and 51% respectively. However, LAR depletion improved insulin-stimulated glucose uptake in myotubes treated with palmitate. Furthermore, the inhibition of LAR prevented palmitate-induced decreases in phosphorylation of IRS1 Tyr632and Akt Ser473 in C2C12 cells. In conclusion, these results reveal that palmitate induces LAR expression in C2C12 cells. We also provided evidence that the inhibition of LAR attenuates palmitate-induced insulin resistance in myotubes.

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Palmitate-induced PTP1B expression is mediated by ceramide-JNK and nuclear factor κB (NF-κB) activation

Cited by 38 publications

References 37 publications

Protein Tyrosine Phosphatase 1B and Insulin Resistance: Role of Endoplasmic Reticulum Stress/Reactive Oxygen Species/Nuclear Factor Kappa B Axis

Protein Tyrosine Phosphatase 1B and Insulin Resistance: Role of Endoplasmic Reticulum Stress/Reactive Oxygen Species/Nuclear Factor Kappa B Axis

Exercise and Glycemic Control: Focus on Redox Homeostasis and Redox-Sensitive Protein Signaling

Leukocyte antigen-related inhibition attenuates palmitate-induced insulin resistance in muscle cells

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